Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30561.m000040 |
Family | CE10 |
Protein Properties | Length: 322 Molecular Weight: 33563.6 Isoelectric Point: 9.2807 |
Chromosome | Chromosome/Scaffold: 30561 Start: 933 End: 1898 |
Description | alpha/beta-Hydrolases superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 56 | 235 | 1.4013e-45 |
LRWQAPQPAAKWQGVRKADHFGARCMQLPLFSDMVFRSDGVSEDCLFLNVWTPAKSAKEKLPVLVYFYGGGFAAGDGSEPRYDGESMAAKGIVTLTVNYR LNVFGFLAHPELTKESPHHASGNYGLMDQAAALQWVKKNIAAFGGDPSRVTIAGESAGSFSVSAQMINPQAKGLIAGAIG |
Full Sequence |
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Protein Sequence Length: 322 Download |
MKKAGLLLLS SSLLALSAHA APRATTATGA VEGVTEASGV TSYKGIPYAA APVGKLRWQA 60 PQPAAKWQGV RKADHFGARC MQLPLFSDMV FRSDGVSEDC LFLNVWTPAK SAKEKLPVLV 120 YFYGGGFAAG DGSEPRYDGE SMAAKGIVTL TVNYRLNVFG FLAHPELTKE SPHHASGNYG 180 LMDQAAALQW VKKNIAAFGG DPSRVTIAGE SAGSFSVSAQ MINPQAKGLI AGAIGESGSL 240 LGLMAPAPLA AAEQAGAAFA QGIGAPALKE LRALPADKLL ENLKKPGAWF FAIQDGYVIP 300 KPPVAMYAAG EQAGCRCWRA GL |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07859 | Abhydrolase_3 | 3.0e-7 | 142 | 234 | 97 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
COG0657 | Aes | 2.0e-7 | 105 | 213 | 110 | + Esterase/lipase [Lipid metabolism] | ||
COG2272 | PnbA | 1.0e-68 | 38 | 314 | 284 | + Carboxylesterase type B [Lipid metabolism] | ||
cd00312 | Esterase_lipase | 1.0e-73 | 38 | 310 | 286 | + Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate. | ||
pfam00135 | COesterase | 2.0e-88 | 40 | 311 | 285 | + Carboxylesterase family. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002536043.1 | 0 | 1 | 322 | 1 | 322 | Para-nitrobenzyl esterase, putative [Ricinus communis] |
RefSeq | YP_003124714.1 | 0 | 28 | 313 | 36 | 324 | Carboxylesterase [Chitinophaga pinensis DSM 2588] |
RefSeq | YP_003385515.1 | 0 | 1 | 313 | 1 | 319 | Carboxylesterase [Spirosoma linguale DSM 74] |
RefSeq | YP_824312.1 | 0 | 18 | 313 | 24 | 321 | carboxylesterase, type B [Solibacter usitatus Ellin6076] |
RefSeq | YP_827738.1 | 0 | 6 | 313 | 1 | 312 | carboxylesterase, type B [Solibacter usitatus Ellin6076] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2ogs_A | 0 | 38 | 315 | 19 | 300 | A Chain A, Crystal Structure Of The Geobacillus Stearothermophilus Carboxylesterase Est55 At Ph 6.2 |
PDB | 2ogt_A | 0 | 38 | 315 | 19 | 300 | A Chain A, Crystal Structure Of The Geobacillus Stearothermophilus Carboxylesterase Est55 At Ph 6.8 |
PDB | 1qe3_A | 0 | 25 | 281 | 7 | 257 | A Chain A, Pnb Esterase |
PDB | 1c7i_A | 0 | 25 | 281 | 7 | 257 | A Chain A, Thermophylic Pnb Esterase |
PDB | 1c7j_A | 0 | 25 | 281 | 7 | 257 | A Chain A, Pnb Esterase 56c8 |
Signal Peptide | |||||
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Cleavage Site | |||||
20 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FN720079 | 198 | 41 | 237 | 5e-40 |
EX962192 | 197 | 38 | 230 | 3e-38 |
JZ193829 | 199 | 40 | 234 | 4e-38 |
FC896521 | 207 | 40 | 237 | 2e-37 |
FC903813 | 199 | 42 | 237 | 1e-36 |
Orthologous Group | |||||
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Species | ID | ||||
Chlamydomonas reinhardtii | Cre02.g105900.t1.2 | ||||
Volvox carteri | Vocar20013658m |
Sequence Alignments (This image is cropped. Click for full image.) |
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